1SHS

SMALL HEAT SHOCK PROTEIN FROM METHANOCOCCUS JANNASCHII


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.90 Å
  • R-Value Free: 0.251 
  • R-Value Work: 0.216 
  • R-Value Observed: 0.216 

wwPDB Validation 3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Crystal structure of a small heat-shock protein.

Kim, K.K.Kim, R.Kim, S.H.

(1998) Nature 394: 595-599

  • DOI: 10.1038/29106
  • Primary Citation of Related Structures:  
    1SHS

  • PubMed Abstract: 
  • The principal heat-shock proteins that have chaperone activity (that is, they protect newly made proteins from misfolding) belong to five conserved classes: HSP100, HSP90, HSP70, HSP60 and the small heat-shock proteins (sHSPs). The sHSPs can form lar ...

    The principal heat-shock proteins that have chaperone activity (that is, they protect newly made proteins from misfolding) belong to five conserved classes: HSP100, HSP90, HSP70, HSP60 and the small heat-shock proteins (sHSPs). The sHSPs can form large multimeric structures and have a wide range of cellular functions, including endowing cells with thermotolerance in vivo and being able to act as molecular chaperones in vitro; sHSPs do this by forming stable complexes with folding intermediates of their protein substrates. However, there is little information available about these structures or the mechanism by which substrates are protected from thermal denaturation by sHSPs. Here we report the crystal structure of a small heat-shock protein from Methanococcus jannaschii, a hyperthermophilic archaeon. The monomeric folding unit is a composite beta-sandwich in which one of the beta-strands comes from a neighbouring molecule. Twenty-four monomers form a hollow spherical complex of octahedral symmetry, with eight trigonal and six square 'windows'. The sphere has an outer diameter of 120 A and an inner diameter of 65 A.


    Related Citations: 
    • Purification, Crystallization, and Preliminary X-Ray Crystallographic Data Analysis of Small Heat Shock Protein Homolog from Methanococcus Jannaschii, a Hyperthermophile
      Kim, K.K., Yokota, H., Santoso, S., Lerner, D., Kim, R., Kim, S.H.
      (1998) J Struct Biol 121: 76
    • Small Heat Shock Protein of Methanococcus Jannaschii, a Hyperthermophile
      Kim, R., Kim, K.K., Yokota, H., Kim, S.H.
      (1998) Proc Natl Acad Sci U S A 95: 9129

    Organizational Affiliation

    Physical Biosciences Division of the Lawrence Berkeley National Laboratory and the Department of Chemistry, University of California at Berkeley, 94720-5230, USA.



Macromolecules
Find similar proteins by:  (by identity cutoff)  |  Structure
Entity ID: 1
MoleculeChainsSequence LengthOrganismDetailsImage
SMALL HEAT SHOCK PROTEINABCDEFGH147Methanocaldococcus jannaschiiMutation(s): 0 
Find proteins for Q57733 (Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440))
Explore Q57733 
Go to UniProtKB:  Q57733
Protein Feature View
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.90 Å
  • R-Value Free: 0.251 
  • R-Value Work: 0.216 
  • R-Value Observed: 0.216 
  • Space Group: H 3
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 171.44α = 90
b = 171.44β = 90
c = 101.98γ = 120
Software Package:
Software NamePurpose
X-PLORmodel building
X-PLORrefinement
DENZOdata reduction
SCALEPACKdata scaling
X-PLORphasing

Structure Validation

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Entry History 

Deposition Data

Revision History 

  • Version 1.0: 1999-07-30
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Derived calculations, Version format compliance